› 2hgs

X-ray diffraction
2.1Å resolution

HUMAN GLUTATHIONE SYNTHETASE

Released:
DOI: 10.2210/pdb2hgs/pdb
PDB entry 2hgs coloured by chain, front view.
PDB entry 2hgs coloured by chain, side view.
PDB entry 2hgs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis of glutathione synthetase deficiency and a rare gene permutation event.
Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW
EMBO J 18 3204-13 (1999)
PMID: 10369661

Function and Biology Details

Reaction catalysed: 
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione synthetase Chain: A
Molecule details ›
Chain: A
Length: 474 amino acids
Theoretical weight: 52.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48637 (Residues: 1-474; Coverage: 100%)
Gene name: GSS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
3 bound ligands:
Ligand MG 2 x MG
Ligand SO4 2 x SO4
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P4122
Unit cell:
a: 84.26Å b: 84.26Å c: 197.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.281
Expression system: Escherichia coli

Quick links

Citations

9 review citations

The ATP-grasp enzymes.
Fawaz et al. (2011)
8 more

25 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
24 more